Enzymatic Ligation of Disulfide-Rich Animal Venom Peptides: Using Sortase A to Form Double-Knotted Peptides

Author(s):  
Poanna Tran ◽  
Christina I. Schroeder
2014 ◽  
Vol 126 (35) ◽  
pp. 9357-9362 ◽  
Author(s):  
Rocco L. Policarpo ◽  
Hansol Kang ◽  
Xiaoli Liao ◽  
Amy E. Rabideau ◽  
Mark D. Simon ◽  
...  
Keyword(s):  

2014 ◽  
Vol 53 (35) ◽  
pp. 9203-9208 ◽  
Author(s):  
Rocco L. Policarpo ◽  
Hansol Kang ◽  
Xiaoli Liao ◽  
Amy E. Rabideau ◽  
Mark D. Simon ◽  
...  
Keyword(s):  

Author(s):  
Stephan Pritz ◽  
Yvonne Wolf ◽  
Oliver Kraetke ◽  
Jana Klose ◽  
Michael Bienert ◽  
...  

2019 ◽  
Vol 476 (24) ◽  
pp. 3835-3847 ◽  
Author(s):  
Aliyath Susmitha ◽  
Kesavan Madhavan Nampoothiri ◽  
Harsha Bajaj

Most Gram-positive bacteria contain a membrane-bound transpeptidase known as sortase which covalently incorporates the surface proteins on to the cell wall. The sortase-displayed protein structures are involved in cell attachment, nutrient uptake and aerial hyphae formation. Among the six classes of sortase (A–F), sortase A of S. aureus is the well-characterized housekeeping enzyme considered as an ideal drug target and a valuable biochemical reagent for protein engineering. Similar to SrtA, class E sortase in GC rich bacteria plays a housekeeping role which is not studied extensively. However, C. glutamicum ATCC 13032, an industrially important organism known for amino acid production, carries a single putative sortase (NCgl2838) gene but neither in vitro peptide cleavage activity nor biochemical characterizations have been investigated. Here, we identified that the gene is having a sortase activity and analyzed its structural similarity with Cd-SrtF. The purified enzyme showed a greater affinity toward LAXTG substrate with a calculated KM of 12 ± 1 µM, one of the highest affinities reported for this class of enzyme. Moreover, site-directed mutation studies were carried to ascertain the structure functional relationship of Cg-SrtE and all these are new findings which will enable us to perceive exciting protein engineering applications with this class of enzyme from a non-pathogenic microbe.


2020 ◽  
Vol 21 (2) ◽  
pp. 97-109 ◽  
Author(s):  
Ana P. dos Santos ◽  
Tamara G. de Araújo ◽  
Gandhi Rádis-Baptista

Venom-derived peptides display diverse biological and pharmacological activities, making them useful in drug discovery platforms and for a wide range of applications in medicine and pharmaceutical biotechnology. Due to their target specificities, venom peptides have the potential to be developed into biopharmaceuticals to treat various health conditions such as diabetes mellitus, hypertension, and chronic pain. Despite the high potential for drug development, several limitations preclude the direct use of peptides as therapeutics and hamper the process of converting venom peptides into pharmaceuticals. These limitations include, for instance, chemical instability, poor oral absorption, short halflife, and off-target cytotoxicity. One strategy to overcome these disadvantages relies on the formulation of bioactive peptides with nanocarriers. A range of biocompatible materials are now available that can serve as nanocarriers and can improve the bioavailability of therapeutic and venom-derived peptides for clinical and diagnostic application. Examples of isolated venom peptides and crude animal venoms that have been encapsulated and formulated with different types of nanomaterials with promising results are increasingly reported. Based on the current data, a wealth of information can be collected regarding the utilization of nanocarriers to encapsulate venom peptides and render them bioavailable for pharmaceutical use. Overall, nanomaterials arise as essential components in the preparation of biopharmaceuticals that are based on biological and pharmacological active venom-derived peptides.


2016 ◽  
Vol 12 (4) ◽  
pp. 205-213 ◽  
Author(s):  
Natalya Voloshchuk ◽  
Danni Liang ◽  
Jun Liang

2011 ◽  
Vol 50 (38) ◽  
pp. 8922-8926 ◽  
Author(s):  
Abu Kausar ◽  
Rosalie D. McKay ◽  
Jade Lam ◽  
Rohan S. Bhogal ◽  
Alexandra Y. Tang ◽  
...  

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